This ebic6 monoclonal antibody reacts with human Epstein-Barr Virus Induced Gene 3 (EBI3). EBI3 can be expressed and secreted as monomers or homodimers, and was first identified in virally-infected B cells. It is also believed to be secreted as a homodimer by cells of the trophoblast, where it may play a role in immune tolerance during pregnancy.

Additionally, EBI3 is a component of two of the four members of the interleukin (IL)-12 family of heterodimeric cytokines. EBI3 was first found to heterodimerize with p28 (IL-30) to form IL-27, which is secreted by antigen-presenting cells in response to pro-inflammatory stimuli. IL-27 has been shown to have both pro-inflammatory and anti-inflammatory effects. It influences the commitment of CD4+ T-cells toward the Th1 lineage by inducing the expression of the T-bet transcription factor and the upregulation of IL-12R beta 2. Its anti-inflammatory functions include the suppression of Th2 and Th17 proliferation and differentiation.

More recently, EBI3 was also found to dimerize with the IL-12 subunit, p35 to form IL-35. The biology of IL-35 is incompletely understood, but it is believed to be unique among the IL-12 family members in its expression and function. It is produced by regulatory T cells, and appears to have immunoregulatory functions. IL-35 has been found to suppress the proliferation and function of effector T cells, and has also been observed to induce a regulatory phenotype on naïve CD4+ cells cultured in its presence.

ELISA results from the culture of human dendritic cells stimulated shown above suggests that at least some of the EBI3 detected by flow is dimerized with p28 to form IL-27. Testing with ebic6 in the context of IL-35 is currently in process. For more information, please contact technical support.